English   español  
Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/110200
COMPARTIR / IMPACTO:
Estadísticas
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:
Título

Structural and mechanistic insights into the association of PKCα-C2 domain to PtdIns(4,5)P2

AutorGuerrero-Valero, Marta; Ferrer-Orta, Cristina ; Querol-Audí, Jordi ; Marín-Vicente, Consuelo; Fita, Ignacio ; Gómez-Fernández, Juan C.; Verdaguer, Núria ; Corbalán-García, Senena
Palabras claveCalcium phosphoinositides
Peripheral membrane proteins
Fecha de publicación21-abr-2009
EditorNational Academy of Sciences (U.S.)
CitaciónProceedings of the National Academy of Sciences of the United States of America 106(16): 6603-6607 (2009)
ResumenC2 domains are widely-spread protein signaling motifs that in classical PKCs act as Ca2+-binding modules. However, the molecular mechanisms of their targeting process at the plasma membrane remain poorly understood. Here, the crystal structure of PKCα-C2 domain in complex with Ca 2+, 1,2-dihexanoyl-sn-glycero-3-[phospho-L-serine] (PtdSer), and 1,2-diayl-sn-glycero-3-[phosphoinositol-4,5-bisphos-phate] [Ptdlns(4,5)P2] shows that PtdSer binds specifically to the calcium-binding region, whereas Ptdlns(4,5)P2 occupies the concave surface of strands β3 and β4. Strikingly, the structure reveals a Ptdlns(4,5)P2-C2 domain-binding mode in which the aromatic residues Tyr-195 and Trp-245 establish direct interactions with the phosphate moieties of the inositol ring. Mutations that abrogate Tyr-195 and Trp-245 recognition of Ptdlns(4,5)P2 severely impaired the ability of PKCα to localize to the plasma membrane. Notably, these residues are highly conserved among C2 domains of topology I, and a general mechanism of C2 domain-membrane docking mediated by Ptdlns(4,5)P 2 is presented.
Versión del editorhttp://dx.doi.org/10.1073/pnas.0813099106
URIhttp://hdl.handle.net/10261/110200
DOI10.1073/pnas.0813099106
Identificadoresdoi: 10.1073/pnas.0813099106
issn: 0027-8424
Aparece en las colecciones: (IBMB) Artículos
Ficheros en este ítem:
Fichero Descripción Tamaño Formato  
accesoRestringido.pdf15,38 kBAdobe PDFVista previa
Visualizar/Abrir
Mostrar el registro completo
 

Artículos relacionados:


NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.